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VEGFR1

From Wikipedia, the free encyclopedia
FLT1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFLT1, FLT, FLT-1, VEGFR-1, VEGFR1, fms related tyrosine kinase 1, vascular endothelial growth factor receptor 1, fms related receptor tyrosine kinase 1
External IDsOMIM: 165070; MGI: 95558; HomoloGene: 134179; GeneCards: FLT1; OMA:FLT1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001159920
NM_001160030
NM_001160031
NM_002019

NM_010228
NM_001363135

RefSeq (protein)

NP_001153392
NP_001153502
NP_001153503
NP_002010

NP_034358
NP_001350064

Location (UCSC)Chr 13: 28.3 – 28.5 MbChr 5: 147.5 – 147.66 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vascular endothelial growth factor receptor 1 is a protein that in humans is encoded by the FLT1 gene.[5]

Function

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FLT1 is a member of VEGF receptor gene family. It encodes a receptor tyrosine kinase which is activated by VEGF-A, VEGF-B, and placental growth factor. The sequence structure of the FLT1 gene resembles that of the FMS (now CSF1R) gene; hence, Yoshida et al. (1987) proposed the name FLT as an acronym for FMS-like tyrosine kinase.[6]

The ablation of VEGFR1 by chemical and genetic means has also recently been found to augment the conversion of white adipose tissue to brown adipose tissue as well as increase brown adipose angiogenesis in mice.[7]

Functional genetic variation in FLT1 (rs9582036) has been found to affect non-small cell lung cancer survival.[8]

Interactions

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FLT1 has been shown to interact with PLCG1[9] and vascular endothelial growth factor B (VEGF-B).[10][11]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102755Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029648Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Shibuya M, Yamaguchi S, Yamane A, Ikeda T, Tojo A, Matsushime H, Sato M (April 1990). "Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family". Oncogene. 5 (4): 519–24. PMID 2158038.
  6. ^ "FLT1 fms related receptor tyrosine kinase 1 [ Homo sapiens (human) ]". National Center for Biotechnology Information.
  7. ^ Seki T, Hosaka K, Fischer C, Lim S, Andersson P, Abe M, Iwamoto H, Gao Y, Wang X, Fong GH, Cao Y (February 2018). "Ablation of endothelial VEGFR1 improves metabolic dysfunction by inducing adipose tissue browning". The Journal of Experimental Medicine. 215 (2): 611–626. doi:10.1084/jem.20171012. PMC 5789413. PMID 29305395.
  8. ^ Glubb DM, Paré-Brunet L, Jantus-Lewintre E, Jiang C, Crona D, Etheridge AS, Mirza O, Zhang W, Seiser EL, Rzyman W, Jassem J, Auman T, Hirsch FR, Owzar K, Camps C, Dziadziuszko R, Innocenti F (July 2015). "Functional FLT1 Genetic Variation is a Prognostic Factor for Recurrence in Stage I-III Non-Small-Cell Lung Cancer". Journal of Thoracic Oncology. 10 (7): 1067–75. doi:10.1097/JTO.0000000000000549. PMC 4494119. PMID 26134224.
  9. ^ Cunningham SA, Arrate MP, Brock TA, Waxham MN (November 1997). "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites". Biochemical and Biophysical Research Communications. 240 (3): 635–9. doi:10.1006/bbrc.1997.7719. PMID 9398617.
  10. ^ Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, Gunji Y, Jeltsch MM, Shibuya M, Alitalo K, Eriksson U (September 1998). "Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells". Proceedings of the National Academy of Sciences of the United States of America. 95 (20): 11709–14. doi:10.1073/pnas.95.20.11709. PMC 21705. PMID 9751730.
  11. ^ Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K (July 1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". The Journal of Biological Chemistry. 274 (30): 21217–22. doi:10.1074/jbc.274.30.21217. PMID 10409677.

Further reading

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